BMRB Entry 11102

Title:
The solution structure of the second thioredoxin domain of human Protein disulfide-isomerase A3
Deposition date:
2010-02-18
Original release date:
2011-02-17
Authors:
Tochio, N.; Koshiba, S.; Inoue, M.; Kigawa, T.; Yokoyama, S.
Citation:

Citation: Tochio, N.; Koshiba, S.; Inoue, M.; Kigawa, T.; Yokoyama, S.. "The solution structure of the second thioredoxin domain of human Protein disulfide-isomerase A3"  .

Assembly members:

Assembly members:
thioredoxin domain, polymer, 142 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:

Experimental source:   Production method: cell free synthesis   Host organism: E. coli - cell free   Vector: P050627-10

Data sets:
Data typeCount
13C chemical shifts611
15N chemical shifts132
1H chemical shifts925

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1thioredoxin domain1

Entities:

Entity 1, thioredoxin domain 142 residues - Formula weight is not available

1   GLYSERSERGLYSERSERGLYPHEASPGLY
2   ASNLEULYSARGTYRLEULYSSERGLUPRO
3   ILEPROGLUSERASNASPGLYPROVALLYS
4   VALVALVALALAGLUASNPHEASPGLUILE
5   VALASNASNGLUASNLYSASPVALLEUILE
6   GLUPHETYRALAPROTRPCYSGLYHISCYS
7   LYSASNLEUGLUPROLYSTYRLYSGLULEU
8   GLYGLULYSLEUSERLYSASPPROASNILE
9   VALILEALALYSMETASPALATHRALAASN
10   ASPVALPROSERPROTYRGLUVALARGGLY
11   PHEPROTHRILETYRPHESERPROALAASN
12   LYSLYSLEUASNPROLYSLYSTYRGLUGLY
13   GLYARGGLULEUSERASPPHEILESERTYR
14   LEUGLNARGGLUALATHRSERGLYPROSER
15   SERGLY

Samples:

sample_1: thioredoxin domain, [U-13C; U-15N], 1.3 mM; d-Tris-HCl 20 mM; NaCl 100 mM; d-DTT 1 mM; NaN3 0.02%; H2O 90%; D2O 10%

condition_1: ionic strength: 120 mM; pH: 7.0; pressure: 1 atm; temperature: 296 K

Experiments:

NameSampleSample stateSample conditions
3D 1H-15N NOESYsample_1isotropiccondition_1
3D 1H-13C NOESYsample_1isotropiccondition_1

Software:

xwinnmr v3.5, Bruker - collection

NMRPipe v20031121, Delaglio, F. - processing

NMRView v5.0.4, Johnson, B.A. - data analysis

Kujira v0.955, Kobayashi, N. - data analysis

CYANA v2.0.17, Guntert, P. - structure solution

NMR spectrometers:

  • Bruker AVANCE 900 MHz

Related Database Links:

PDB
DBJ BAG56782
GB ACA57910 EQB77541
REF XP_004056140

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks